ArticleMicrobial biotechnology2011
Bioengineering of a Nisin A-producing Lactococcus lactis to create isogenic strains producing the natural variants Nisin F, Q and Z.
Article in Microbial biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 98 citations in OpenAlex.
- From predicted bacteriocins to ecological function.Current research in microbial sciences · 2026Review
- Genomic Analysis of Bacteriocin-Producing Staphylococci: High Prevalence of Lanthipeptides and the Micrococcin P1 Biosynthetic Gene Clusters.Probiotics and antimicrobial proteins · 2025Article
- Bacteriocins from Lactic Acid Bacteria Could Modulate the Wnt Pathway: A Possible Therapeutic Candidate for the Management of Colorectal Cancer- AnAnti-cancer agents in medicinal chemistry · 2025Article
- In Bacterial Membranes Lipid II Changes the Stability of Pores Formed by the Antimicrobial Peptide Nisin.The journal of physical chemistry. B · 2024Article
- A Staphylococcus capitis strain with unusual bacteriocin production.Microbial biotechnology · 2023Article
- Probiotic-Derived Bioactive Compounds in Colorectal Cancer Treatment.Microorganisms · 2023Review
- Engineering of Nisin as a Means for Improvement of Its Pharmacological Properties: A Review.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Anti-inflammatory and wound healing properties of lactic acid bacteria and its peptides.Folia microbiologica · 2023Review
- Bioengineering of a Lactococcus lactis subsp. lactis strain enhances nisin production and bioactivity.PloS one · 2023Article
- Multi-Omics Approach in Amelioration of Food Products.Frontiers in microbiology · 2022Review
- Probiotics for periodontal health-Current molecular findings.Periodontology 2000 · 2021Review
- Distribution and Diversity of Nisin Producing LAB in Fermented Food.Current microbiology · 2021Article
- Semisynthetic Macrocyclic Lipo-lanthipeptides Display Antimicrobial Activity Against Bacterial Pathogens.ACS synthetic biology · 2021Article
- Nisin- and Ripcin-Derived Hybrid Lanthipeptides Display Selective Antimicrobial Activity againstACS synthetic biology · 2021Article
- Review: Lessons Learned From Clinical Trials Using Antimicrobial Peptides (AMPs).Frontiers in microbiology · 2021Review
- Application of bacteriocins in food preservation and infectious disease treatment for humans and livestock: a review.RSC advances · 2020Review
- Migration of Bacteriocins Across Gastrointestinal Epithelial and Vascular Endothelial Cells, as Determined Using In Vitro Simulations.Scientific reports · 2019Article
- Article
- Discovery of a novel lantibiotic nisin O from Blautia obeum A2-162, isolated from the human gastrointestinal tract.Microbiology (Reading, England) · 2017Article
- Efficacy of Lantibiotic Treatment of Staphylococcus aureus-Induced Skin Infections, Monitored by In Vivo Bioluminescent Imaging.Antimicrobial agents and chemotherapy · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nisin is the prototypical example of the lantibiotic family of antimicrobial peptides and has been employed as a food preservative for over half a century. It has also attracted attention due to its potency against a number of multidrug-resistant clinical pathogens. Nisin A is the originally isolated form of Nisin and a further five natural variants have been described which differ by up to 10 amino acids (of 34 in total in Nisin A). Nisins A, Z, F and Q are produced by Lactococcus lactis, while Nisins U and U2 are produced by Streptococcus sp. In this study we bioengineered the nisA gene of a Nisin A producer to generate genes encoding Nisins Z, F, Q, U and U2. We determined that while active Nisin Z, F and Q can be produced against this genetic background, active forms of Nisin U and U2 are not generated. Minimum inhibitory concentration studies with Nisin A, Z, F and Q variants against a series of different clinically significant pathogens establish differences in specific activities against selected targets. Nisin F was most impressive, being the most active, or one of the most active, against the MRSA strain ST 525, EC 676, EC 725, VISA 22900, VISA 22781, hVISA 35197, Staphylococcus aureus 8325-4 and L. lactis HP. Nisin Z was most active against ST 299, hVISA 32683 and, together with Nisin F, HP but had contrastingly poor activity against ST 525, EC 676 and 8325-4. Nisin F, Q and A exhibited similar potency against VISA 22900. This was the only target against which Nisin Q and Nisin A were among the most active variants.
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